PRM1_CANGA
ID PRM1_CANGA Reviewed; 622 AA.
AC Q6FNX1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; OrderedLocusNames=CAGL0J08371g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Involved in cell fusion during mating by stabilizing the
CC plasma membrane fusion event. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PRM1 family. {ECO:0000305}.
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DR EMBL; CR380956; CAG61024.1; -; Genomic_DNA.
DR RefSeq; XP_448073.1; XM_448073.1.
DR AlphaFoldDB; Q6FNX1; -.
DR STRING; 5478.XP_448073.1; -.
DR EnsemblFungi; CAG61024; CAG61024; CAGL0J08371g.
DR GeneID; 2889705; -.
DR KEGG; cgr:CAGL0J08371g; -.
DR CGD; CAL0133330; CAGL0J08371g.
DR VEuPathDB; FungiDB:CAGL0J08371g; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; Q6FNX1; -.
DR OMA; AYITSER; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IEA:EnsemblFungi.
DR InterPro; IPR026777; PRM1.
DR PANTHER; PTHR31030; PTHR31030; 1.
PE 3: Inferred from homology;
KW Cell membrane; Conjugation; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337275"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..288
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..590
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 70202 MW; DB3F2CE1C6A60F4E CRC64;
MRNYLLLRDR LTQVWLNKYS ITVTILTAKI VLFNYFIIRI LRYTEKYAIS SCNGLDQVNR
KVYDDLPIFV NTLGNYMIRK SMLESVEASL RGLEILIDAS EGLLGFLVDL YLGTYACLLI
SAVDGAVDVA TNTTEHILEA VNNTLIEATR GLDDGLNDLT SLINKGGNRL SSIFKSDNSV
AASLSKVNFT VKGLRNIHLS SKINDQLQYM ADKVPSFDDL KSETKDLISI PFYHVKREIT
KVNAESLLPD TKILYLRNNT DTTLYPICGQ YIPNIKKVYE HLIHILKVGN ILVAILGIFI
ALFMAIPSIQ KEYQESKRLN NVQDEVSQYI DNKEFMSSGD NSSLNYSPFN DSKFNLAESY
QRNFNPIARW MTIKMGKYFG NDETEYSERL QFCMLYIFSS RSSTIMAMGL IGLITVAIQL
IVIQIISNYL SNTGKVHIQL QASNDEINKM IKSDINLWTS LANQYVNGTE ANLNTQVFGW
ITNTTASVNA TVAHAVDKIE YILASSFNNT PLYKPMKTVV GCAILRKLIS VENAMTWINN
EAHIKLPRIN TTELINIAGH TKMLPSSNES HMFDQVEKIV NIARKTALNE LYVPLALIGI
WLTQIPMALL LSWRRCDTTG KT
